Cyclophilin



Cyclophilin (Cyp) binds cyclosporin. They are peptidylprolyl isomerases which catalyze the isomerisation of proline. The Cyp-A/cyclosporin A complex inhibits organ rejection. Cyp-D is a component of the mitochondria permeability pore. Rotamase such as FKBP is a prokaryotic Cyp which is not inhibited by cyclosporin but by FK-506 – an immunosuppressive drug. The images at the left and at the right correspond to one representative Cyclophilin, i.e. crystal structure of human Cyclophilin A (2x25).

Cyclophilin-A
2x25, 2x2a, 3k0m, 3k0n, 1w8l, 1w8m, 1w8v, 1rmh, 2cpl – hCyp-A – human

1oca – hCyp-A - NMR

3k0o, 3k0p, 3k0q, 3k0r, 2alf – hCyp-A (mutant)

2a2c, 1cwa, 1cwb, 1cwc – hCyp-A+cyclosporin A

3cys - hCyp-A+cyclosporin A - NMR

1cwj, 1bck, 1cwi, 1cwo, 1cwf, 1cwh, 1cwk, 1cwl, 1cwm, 1mik - hCyp-A+cyclosporin A derivative

2rma, 2rmb - hCyp-A+cyclosporin A+cyclosporin A derivative

1mf8, 1m63 - hCyp-A+cyclosporin A+ calcineurin subunits A,B

3odi, 3odl – hCyp-A+voclosporin

2x2d, 1m9c, 1m9d, 1m9e, 1m9f, 1m9x, 1m9y, 1awq, 1awr, 1aws, 1awt, 1awu, 1awv, 1ak4, 1fgl - hCyp-A+HIV-1 N-terminal capsid domain

1zkf – hCyp-A+suc-AGPF-pNA

1ynd, 1nmk – hCyp-A+ sanglifehrin

2cyh, 3cyh, 4cyh, 5cyh - hCyp-A+dipeptide

1vbs, 1vbt – hCyp-A+tetrapeptide

1vdn – yCyp-A+peptidyl coumarin – yeast

1ist – yCyp-A

1w74 – Cyp-A – Mycobacterium tuberculosis

1lop - EcCyp-A+peptidyl nitroanilide - Escherichia coli

1csa – EcCyp-A+ cyclosporin A – NMR

2xgy – Cyp-A+RELIK capsid N-terminal - rabbit

Cyclophilin-B
3ich – hCyp-B

3ici - hCyp-B+calmegin fragment

1v9t – EcCyp-B+peptidyl nitroanilide

1vai - EcCyp-B+peptidyl coumarin

1cyn – hCyp-B +cyclosporin A derivative

1j2a – EcCyp-B (mutant)

Cyclophilin-C
2esl - hCyp-C+cyclosporin A

2rmc - Cyp-C+cyclosporin A – mouse

Cyclophilin-D
2bit – hCyp-D

2viu – hCyp-D+DMSO

2z6w - hCyp-D+cyclosporin A

Cyclophilin-E
2kyx, 1zmf – hCyp-E PPIASE domain

2r99 - hCyp-E ABH-like domain

2cqb – hCyp-E RNA recognition motif

2ck1, 2cmt – Cyp-E – Schistosoma  mansoni

2kyx – hCyp-E RRM domain – NMR

3lpy, 3mdf - hCyp-E RRM domain

Cyclophilin-G
2wfi, 2gw2 - hCyp-G PPIASE domain

2wfj - hCyp-G PPIASE domain+cyclosporin A

Cyclophilin-H
1mzw – hCyp-H+peptide

Cyclophilin-J
2ok3, 1xyh - hCyp-J

2oju - hCyp-J+cyclosporin A

Cyclophilin-3
2igv, 2igw, 1e8k – CeCyp-3+dipeptide – Caenorhabditis elegans

1dyw - CeCyp-3

1e3b – CeCyp-3+AUP(ET)3

Cyclophilin-5
1h0p – CeCyp-5 (mutant)

Cyclophilin-40
1ihg, 1iip – Cyp-40 – bovine

Cyclophilin
3bo7 - TgCyp+cyclosporin A - Toxoplasma gondii

2nul – EcCyp

1clh – EcCyp – NMR

1qoi – hCyp SNUCYP-20

3k2c – Cyp – Encephalitozoon cuniculi

3eov - LdCyp+cyclosporin A – Leishmania donovani

3bt8 – LdCyp

2haq – LdCyp-A

2hqj – Cyp – Leishmania major

3bkp – TgCyp

2cfe – Cyp – Malassezia sympodialis

2c3b – Cyp – Aspergillus fumigatus

1z81 – Cyp – Plasmodium Yoelli

1qng – PfCyp+cyclosporin A – Plasmodium falciparum

1qnh – PfCyp (mutant)+cyclosporin A

1xo7 – TcCyp – Trypanosoma cruzi

1xq7 - TcCyp+cyclosporin A

1a58 - Cyp – Brugia malayi

2ko7 – BpCyp+inhibitor – Burkholderia pseudomallei

2ke0 – BpCyp – NMR

Rotamase (FKBP)
1fks, 1fkt, 1fkr, 2kfw – EcFKBP – NMR

1q6h, 1q6u – EcFKBP

1q6i – EcFKBP+FK-506

3jxv, 3jym – FKBP73 – wheat

3mdy – hFKBP-1A+BMPR1B

3h9r - hFKBP-1A+ activin receptor type I

1j4r – hFKBP-1+FKB-001

2ppp, 2ppn, 2dg3, 1d6o – hFKBP-12

2ppo – hFKBP-12 (mutant)

2dg4, 1fkb - hFKBP-12+rapamycin

2fap, 1nsg, 1fap - hFKBP-12+rapamycin+FRB

1f40 - hFKBP-12+GPI-1046

1a7x – hFKBP-12+FK-1012

1d7h, 1d7i, 1d7j, 1fkg, 1fkh, 1fki - hFKBP-12+ligand

2dg9 - hFKBP-12 (mutant)+rapamycin

1fkl - cFKBP-12+rapamycin - cow

2pbc - hFKBP-13

1y0o, 1u79 – AtFKBP-13 - Arabidopsis thaliana

2kfv – hFKBP-25 N-terminal

2vn1 – PfFKBP-35 FK506-binding domain+FK506

3b7x – hFKBP-36

2if4 – AtFKBP

2f4e - AtFKBP-42 N-terminal

1kt0, 1kt1 – hFKBP-51 (mutant)

1ix5 – FKBP – Methanothermococcus thermolithotrophicus – NMR

1bl4 – hFKBP (mutant)+inhibitor

1bkf – hFKBP (mutant)+FK-506

1fkf - hFKBP+FK-506

1fkr, 1fks, 1fkt – hFKBP - NMR